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Aldehyde Dehydrogenase의 반응 메카니즘에 관한 연구 -Dehydrogenase 활성의 속도결정 단계의 추구-
주충노,김두식,구현서,김주휘,Joo, Chung-No,Kim, Doo-Shik,Koo, Hyon-Seo,Kim, Joo-Hwee 생화학분자생물학회 1992 한국생화학회지 Vol.25 No.6
소의 간 aldehyde dehydrogenase(ALDH)와 사람 적혈구 ALDH에 미치는 금속이온의 영향과 화학변형 실험을 행하고 보고된 ALDH의 반응 메카니즘에 관한 실험결과들을 종합하여 광범위한 특이성을 가진 일반 ALDH의 dehydrogenase 활성의 속도제한 단계가 Enzyme-NADH complex로부터의 NADH의 해리단계임을 알 수 있었다. The effect of several ions and chemical modification experiments using bovine liver cytosolic aldehyde dehydrogenase (ALDH) and human erythrocyte ALDH have been carried out to understand the rate-limiting process of dehydrogenase activity. From the previously reported experimental results and this study suggested that the releasing step of NADH from Enzyme-NADH complex might be a rate-limiting process.
Aldehyde Dehydrogenase 의 반응 메카니즘에 관한 연구 - Dehydrogenase 활성의 속도결정 단계의 추구
주충노,김두식,구현서,김주희 ( Chung No Joo,Doo Shik Kim,Hyon Seo Koo,Joo Hwee Kim ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.6
The effect of several ions and chemical modification experiments using bovine liver cytosolic aldehyde dehydrogenase (ALDH) and human erythrocyte ALDH have been carried out to understand the rate-limiting process of dehydrogenase activity. From the previously reported experimental results and this study suggested that the releasing step of NADH from Enzyme-NADH complex might be a rate-limiting process.
사람 적혈구 알데히드 탈수소효소의 정제와 특성에 관한 연구
김주희,주충노 ( Joo Hwee Kim,Chung No Joo ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.5
Aldehyde dehydrogenase (ALDH) isozymes of human erythrocyte were separated and purified. ALDH having low K_m value (74.6 μM) and high K_m value (174 μM) for acetaldehydde were named low K_m, ALDH and high K_m ALDH respectively. For low K_m, ALDH, both NAD^+ and NADP+ could be used as coenzyme, but high K_m ALDH used only NAD^+. Their molecular weights were determined according to pore-gradient polyacrylamide gel electrophoresis and found that low K_m ALDH was 269,000 dalton and high K_m, ALDH 273,000 dalton. SDS-polyacrylamide gel electrophoresis showed that they were both homotetramer, composed of four identical subunits. The molecular weight of subunit of these two isozymes were 59,500 and 60,600 dalton respectively. Both, high K_m and low K_m ALDH showed esterase activity as well as dehydrogenase activity. They were very stable at 35℃ and optimum pH of both isozymes were 9.5. isoelectric point of low K_m ALDH was 5.5.